LATS2_MOUSE
ID LATS2_MOUSE Reviewed; 1042 AA.
AC Q7TSJ6; Q8CDJ4; Q9JMI3;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Serine/threonine-protein kinase LATS2;
DE EC=2.7.11.1;
DE AltName: Full=Kinase phosphorylated during mitosis protein;
DE AltName: Full=Large tumor suppressor homolog 2;
DE AltName: Full=Serine/threonine-protein kinase kpm;
GN Name=Lats2 {ECO:0000312|EMBL:AAH53028.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA92380.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Testis {ECO:0000269|PubMed:10673337};
RX PubMed=10673337; DOI=10.1006/geno.1999.6065;
RA Yabuta N., Fujii T., Copeland N.G., Gilbert D.J., Jenkins N.A.,
RA Nishiguchi H., Endo Y., Toji S., Tanaka H., Nishimune Y., Nojima H.;
RT "Structure, expression, and chromosome mapping of LATS2, a mammalian
RT homologue of the Drosophila tumor suppressor gene lats/warts.";
RL Genomics 63:263-270(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000312|EMBL:AAH53028.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH53028.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH53028.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15343267; DOI=10.1038/sj.emboj.7600371;
RA McPherson J.P., Tamblyn L., Elia A., Migon E., Shehabeldin A.,
RA Matysiak-Zablocki E., Lemmers B., Salmena L., Hakem A., Fish J., Kassam F.,
RA Squire J., Bruneau B.G., Hande M.P., Hakem R.;
RT "Lats2/Kpm is required for embryonic development, proliferation control and
RT genomic integrity.";
RL EMBO J. 23:3677-3688(2004).
RN [5]
RP STRUCTURE BY NMR OF 98-138.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-038, a UBA domain from mouse LATS2 (large
RT tumor suppressor homolog 2).";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Negative regulator of YAP1 in the Hippo signaling pathway
CC that plays a pivotal role in organ size control and tumor suppression
CC by restricting proliferation and promoting apoptosis. The core of this
CC pathway is composed of a kinase cascade wherein STK3/MST2 and
CC STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates
CC and activates LATS1/2 in complex with its regulatory protein MOB1,
CC which in turn phosphorylates and inactivates YAP1 oncoprotein and
CC WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation
CC into the nucleus to regulate cellular genes important for cell
CC proliferation, cell death, and cell migration. Acts as a tumor
CC suppressor which plays a critical role in centrosome duplication,
CC maintenance of mitotic fidelity and genomic stability. Negatively
CC regulates G1/S transition by down-regulating cyclin E/CDK2 kinase
CC activity. Negative regulator of the androgen receptor. Phosphorylates
CC SNAI1 in the nucleus leading to its nuclear retention and
CC stabilization, which enhances its epithelial-mesenchymal transition and
CC tumor cell invasion/migration activities. This tumor-promoting activity
CC is independent of its effects upon YAP1 or WWTR1/TAZ (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:15343267}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q9NRM7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9NRM7};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with and is phosphorylated by AURKA. Binds to AR (By
CC similarity). Interacts with AJUBA during mitosis and this complex
CC regulates organization of the spindle apparatus through recruitment of
CC gamma-tubulin to the centrosome. Interacts (via PPxY motif) with YAP1
CC (via WW domains). Interacts with MOB1A and MOB1B (By similarity).
CC Interacts with LIMD1, WTIP and AJUBA (By similarity). Interacts with
CC SNAI1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:15343267}. Cytoplasm
CC {ECO:0000269|PubMed:15343267}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:15343267}. Nucleus {ECO:0000250}. Note=Colocalizes
CC with AURKA at the centrosomes during interphase, early prophase and
CC cytokinesis (By similarity). Migrates to the spindle poles during
CC mitosis, and to the midbody during cytokinesis. Translocates to the
CC nucleus upon mitotic stress by nocodazole treatment (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in ovary and testis and at
CC lower levels in all other tissues examined.
CC {ECO:0000269|PubMed:10673337}.
CC -!- PTM: Autophosphorylated and phosphorylated during M-phase and the G1/S-
CC phase of the cell cycle. Phosphorylated and activated by STK3/MST2.
CC Phosphorylation by NUAK2 may regulate its activity in phosphorylation
CC and inactivation YAP1. {ECO:0000250|UniProtKB:Q9NRM7}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC26704.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB023958; BAA92380.1; -; mRNA.
DR EMBL; AK029966; BAC26704.1; ALT_FRAME; mRNA.
DR EMBL; BC053028; AAH53028.1; -; mRNA.
DR CCDS; CCDS27158.1; -.
DR RefSeq; NP_056586.2; NM_015771.2.
DR PDB; 2COS; NMR; -; A=98-138.
DR PDBsum; 2COS; -.
DR AlphaFoldDB; Q7TSJ6; -.
DR SMR; Q7TSJ6; -.
DR BioGRID; 206050; 1.
DR CORUM; Q7TSJ6; -.
DR IntAct; Q7TSJ6; 123.
DR MINT; Q7TSJ6; -.
DR STRING; 10090.ENSMUSP00000022531; -.
DR iPTMnet; Q7TSJ6; -.
DR PhosphoSitePlus; Q7TSJ6; -.
DR MaxQB; Q7TSJ6; -.
DR PaxDb; Q7TSJ6; -.
DR PRIDE; Q7TSJ6; -.
DR ProteomicsDB; 290010; -.
DR DNASU; 50523; -.
DR Ensembl; ENSMUST00000022531; ENSMUSP00000022531; ENSMUSG00000021959.
DR GeneID; 50523; -.
DR KEGG; mmu:50523; -.
DR UCSC; uc007udk.1; mouse.
DR CTD; 26524; -.
DR MGI; MGI:1354386; Lats2.
DR VEuPathDB; HostDB:ENSMUSG00000021959; -.
DR eggNOG; KOG0608; Eukaryota.
DR GeneTree; ENSGT00940000159161; -.
DR HOGENOM; CLU_004885_1_2_1; -.
DR InParanoid; Q7TSJ6; -.
DR OMA; EPLAYMA; -.
DR OrthoDB; 759391at2759; -.
DR PhylomeDB; Q7TSJ6; -.
DR TreeFam; TF351549; -.
DR Reactome; R-MMU-2028269; Signaling by Hippo.
DR BioGRID-ORCS; 50523; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Lats2; mouse.
DR EvolutionaryTrace; Q7TSJ6; -.
DR PRO; PR:Q7TSJ6; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q7TSJ6; protein.
DR Bgee; ENSMUSG00000021959; Expressed in ascending aorta and 251 other tissues.
DR ExpressionAtlas; Q7TSJ6; baseline and differential.
DR Genevisible; Q7TSJ6; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IGI:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0035329; P:hippo signaling; IGI:MGI.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0001827; P:inner cell mass cell fate commitment; IGI:MGI.
DR GO; GO:0001828; P:inner cell mass cellular morphogenesis; IGI:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0030216; P:keratinocyte differentiation; IGI:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:MGI.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IMP:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IDA:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0046620; P:regulation of organ growth; IMP:MGI.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR028742; LATS2.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR24356:SF149; PTHR24356:SF149; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Kinase; Magnesium; Metal-binding; Mitosis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Tumor suppressor.
FT CHAIN 1..1042
FT /note="Serine/threonine-protein kinase LATS2"
FT /id="PRO_0000086235"
FT DOMAIN 97..138
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 626..931
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 932..1010
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 23..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 472..475
FT /note="PPxY motif"
FT COMPBIAS 27..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 749
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P22612,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 632..640
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22612,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 655
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NRM7,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 82
FT /note="Phosphoserine; by AURKA"
FT /evidence="ECO:0000250|UniProtKB:Q9NRM7"
FT MOD_RES 267
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRM7"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRM7"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRM7"
FT MOD_RES 999
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRM7"
FT CONFLICT 184
FT /note="Q -> R (in Ref. 1; BAA92380)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="Q -> R (in Ref. 2; BAC26704)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="E -> K (in Ref. 2; BAC26704)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="M -> V (in Ref. 1; BAA92380)"
FT /evidence="ECO:0000305"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:2COS"
FT HELIX 113..123
FT /evidence="ECO:0007829|PDB:2COS"
FT HELIX 128..138
FT /evidence="ECO:0007829|PDB:2COS"
SQ SEQUENCE 1042 AA; 115472 MW; 7E0E73A73DB954C0 CRC64;
MRPKTFPATT YSGNSRQRLQ EIREGLKQPS KASTQGLLVG PNSDTSLDAK VLGSKDASRQ
QQMRATPKFG PYQKALREIR YSLLPFANES GTSAAAEVNR QMLQELVNAG CDQEMAGRAL
KQTGSRSIEA ALEYISKMGY LDPRNEQIVR VIKQTSPGKG LAPTPVTRRP SFEGTGEALP
SYHQLGGANY EGPAALEEMP RQYLDFLFPG AGAGTHGAQA HQHPPKGYST AVEPSAHFPG
THYGRGHLLS EQPGYGVQRS SSFQNKTPPD AYSSMAKAQG GPPASLTFPA HAGLYTASHH
KPAATPPGAH PLHVLGTRGP TFTGESSAQA VLAPSRNSLN ADLYELGSTV PWSAAPLARR
DSLQKQGLEA SRPHVAFRAG PSRTNSFNNP QPEPSLPAPN TVTAVTAAHI LHPVKSVRVL
RPEPQTAVGP SHPAWVAAPT APATESLETK EGSAGPHPLD VDYGGSERRC PPPPYPKHLL
LPSKSEQYSV DLDSLCTSVQ QSLRGGTEQD RSDKSHKGAK GDKAGRDKKQ IQTSPVPVRK
NSRDEEKRES RIKSYSPYAF KFFMEQHVEN VIKTYQQKVS RRLQLEQEMA KAGLCEAEQE
QMRKILYQKE SNYNRLKRAK MDKSMFVKIK TLGIGAFGEV CLACKLDTHA LYAMKTLRKK
DVLNRNQVAH VKAERDILAE ADNEWVVKLY YSFQDKDSLY FVMDYIPGGD MMSLLIRMEV
FPEHLARFYI AELTLAIESV HKMGFIHRDI KPDNILIDLD GHIKLTDFGL CTGFRWTHNS
KYYQKGNHMR QDSMEPGDLW DDVSNCRCGD RLKTLEQRAQ KQHQRCLAHS LVGTPNYIAP
EVLLRKGYTQ LCDWWSVGVI LFEMLVGQPP FLAPTPTETQ LKVINWESTL HIPTQVRLSA
EARDLITKLC CAADCRLGRD GADDLKAHPF FNTIDFSRDI RKQPAPYVPT ISHPMDTSNF
DPVDEESPWH EASGESAKAW DTLASPSSKH PEHAFYEFTF RRFFDDNGYP FRCPKPSEPA
ESADPGDADL EGAAEGCQPV YV
